Recombinant Human LAG-3 Fc Chimera Avi-tag Protein, CF

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When Recombinant Human Hepassocin/FGL1 His-tag (Catalog # 10285-HE) is immobilized at 1 μg/mL (100 μL/well), the concentration of Recombinant Human LAG-3 Fc Chimera Avi-tag that produces 50% of the optimal ...read more
2 μg/lane of Biotinylated Recombinant Human LAG-3 Fc Chimera Avi-tag (Catalog # AVI2319) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human LAG-3 Fc Chimera Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Hepassocin/FGL1 His-tag (Catalog # 10285-HE) is immobilized at 1 μg/mL (100 μL/well), the concentration of Recombinant Human LAG‑3 Fc Chimera Avi-tag that produces 50% of the optimal binding response is 0.1-0.6 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human LAG-3 protein
Human LAG-3
(Leu23-Leu450)
Accession # P18627.5
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Leu23
Structure / Form
Disulfide-linked homodimer, biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
75 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
81-92 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human LAG-3 Fc Chimera Avi-tag Protein, CF

  • CD223 antigen
  • CD223
  • LAG3
  • LAG-3
  • lymphocyte activating 3
  • lymphocyte activation gene 3 protein
  • lymphocyte-activation gene 3
  • Secreted lymphocyte activation gene 3 protein
  • sLAG-3

Background

LAG-3 (Lymphocyte activation gene-3), designated CD223, is a 70 kDa type I transmembrane protein that is a member of the immunoglobulin superfamily (IgSF) (1, 2). LAG-3 shares approximately 20% amino acid sequence homology with CD4, but has similar structure and binds to MHC class II with higher affinity, providing negative regulation of T cell receptor signaling (1, 2). Human LAG-3 cDNA encodes 525 amino acids (aa) that include a 28 aa signal sequence, a 422 aa extracellular domain (ECD) with four Ig-like domains, a  transmembrane region and a highly charged cytoplasmic region. Within the ECD, human LAG-3 shares 70%, 67%, 76%, and 73% aa sequence identity with mouse, rat, porcine, and bovine LAG-3, respectively. LAG-3 is expressed on activated CD4+ and CD8+ T cells, NK cells, and plasmacytoid dendritic cells (pDC), but not on resting T cells (1-3). LAG-3 on activated CD4+CD25+ Treg cells plays a role in their suppressive activity (4). LAG-3 limits the expansion of activated T cells and pDC in response to selected stimuli (3-5). A soluble 54 kDa form, sLAG-3, can be shed by metalloproteinases ADAM10 and TACE/ADAM17 (6, 7). While monomeric sLAG-3 itself may be inactive, shedding allows for normal T cell activation by removing negative regulation (7). Binding of a homodimerized sLAG-3/Ig fusion protein to MHC class II molecules induces maturation of immature DC, and secretion of cytokines such as IFN-gamma and TNF-alpha by type 1 cytotoxic CD8+ T cells and NK cells (8, 9). sLAG-3/Ig has been used as a potential adjuvant to stimulate a cytotoxic anti-cancer immune response (9, 10). In mice, deletion of LAG-3 and another negative regulator, PD-1, facilitates anti-cancer response but also blocks self-tolerance and increases susceptibility to autoimmune diseases (11, 12). In humans, antibody-mediated down‑regulation of LAG-3 and PD-1 allows more effective control of chronic malaria, while in NOD (non‑obese diabetic) mice, deletion of LAG-3 alone accelerates diabetes (12-14).

  1. Triebel, F. et al. (1990) J. Exp. Med. 171:1393.
  2. Baixeras, E. et al. (1992) J. Exp. Med 176:327.
  3. Workman, C.J. et al. (2004) J. Immunol. 172:5450.
  4. Huang, C.T. et al. (2004) Immunity 21:503.
  5. Workman, C.J. et al. (2009) J. Immunol. 182:1885.
  6. Li, N. et al. (2004) J. Immunol. 173:6806.
  7. Li, N. et al. (2007) EMBO J. 26:494.
  8. Andreae, S. et al. (2003) Blood 102:2130.
  9. Brignone, C. et al. (2007) J. Immunol. 179:4202.
  10. Brignone, C. et al. (2010) J. Transl. Med. 8:71.
  11. Woo, S.R. et al. (2011) Cancer Res. 72:917.
  12. Okazaki, T. et al. (2011) J. Exp. Med. 208:395.
  13. Bettini, M. et al. (2011) J. Immunol. 187:3493.
  14. Butler, N.S. et al. (2012) Nat. Immunol. 13:188.

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